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2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispd) from arabidopsis thaliana

Analyse 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispd) from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W77
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase
EC: 2.7.7.60
UniProt: O64726
Ligands: C5P, CU, CD
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60)	protein	212	33% helix, 24% strand	O64726

Ligands and binding sites

C5P · Cytidine-5'-monophosphate · ligand · chains A
CU · Copper (II) ion · metal · 4 copies · chains A
CD · Cadmium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	227	0.56	0.78	44	C5P

Compared structures

1W77 · 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O64726
Elsewhere: RCSB PDB 1W77 · PDBe 1W77 · UniProt O64726

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